The objective of this research was to characterize chemically the plastein produced from a pancreatic hydrolysate of soy protein isolate (SPI). The SPI hydrolysate was obtained by an enzymatic discontinuous process, with a 5% substrate concentration, an enzyme/substrate ratio of 1/20, 37ºC, 6 hours under constant stirring. The plastein was produced from this hydrolysate with a 40% substrate (w/v), pH 7, 37ºC, for 24 hours without stirring. The protein profile was analyzed by gel electrophoresis (SDS-PAGE) and by molecular exclusion chromatography (MEC). The SDS-PAGE did not permit the bands visualization. The MEC pointed that the SPI hydrolysate presented 5 zones in the region between 5.4 and 66.2 kDa while plastein presented 2 zones in the MW of 9.6 and 58.7 kDa. The amino acid scoring showed that the limiting amino acids were the sulfur-containing amino acids; reference values of 93.2 and 96.4% were observed for the hydrolysate and plastein, respectively. The enzymatic modification through the plastein synthesis reaction showed to be a viable process for production of raw material in food formulation for clinical nutrition and other systems, but it should be supplemented when used exclusive source protein.
plastein; enzymatic hydrolysis; pancreatin; soy protein isolate; molecular weight; amino acid scoring
